David A. Moffet

ORCID: 0000-0002-7430-861X
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Research Areas
  • Alzheimer's disease research and treatments
  • Endoplasmic Reticulum Stress and Disease
  • Chemical Synthesis and Analysis
  • Carbohydrate Chemistry and Synthesis
  • Amyloidosis: Diagnosis, Treatment, Outcomes
  • Biochemical and Structural Characterization
  • Drug Transport and Resistance Mechanisms
  • Prion Diseases and Protein Misfolding
  • Hemoglobin structure and function
  • Diet and metabolism studies
  • Biochemical and Molecular Research
  • Pancreatitis Pathology and Treatment
  • Pancreatic function and diabetes
  • Biofuel production and bioconversion
  • Advanced Glycation End Products research
  • Nanocluster Synthesis and Applications
  • Liver Disease Diagnosis and Treatment
  • Plant-Microbe Interactions and Immunity
  • Photosynthetic Processes and Mechanisms
  • Supramolecular Self-Assembly in Materials
  • Heme Oxygenase-1 and Carbon Monoxide
  • Phytase and its Applications
  • Amino Acid Enzymes and Metabolism
  • Folate and B Vitamins Research
  • Neonatal Health and Biochemistry

Loyola Marymount University
2011-2024

In-Q-Tel
2009

Brown University
2005

Princeton University
2000-2003

Abstract Binary patterning of polar and nonpolar amino acids has been used as the key design feature for constructing large combinatorial libraries de novo proteins. Each position in a binary patterned sequence is designed explicitly to be either or nonpolar; however, precise identities these are varied extensively. The underpinnings “binary code” strategy preclude explicit particular side chains at specified positions. Therefore, packing interactions cannot priori. To assess whether code...

10.1110/ps.0228003 article EN Protein Science 2003-01-01

ADVERTISEMENT RETURN TO ISSUEPREVCommunicationNEXTPeroxidase Activity in Heme Proteins Derived from a Designed Combinatorial LibraryDavid A. Moffet, Laura K. Certain, Allison J. Smith, Adam Kessel, Katharine Beckwith, and Michael H. HechtView Author Information Department of Chemistry, Princeton University Princeton, New Jersey 08544-1009 Cite this: Am. Chem. Soc. 2000, 122, 31, 7612–7613Publication Date (Web):July 21, 2000Publication History Received6 April 2000Published online21 July...

10.1021/ja001198q article EN Journal of the American Chemical Society 2000-07-21

The aggregation of the 37-residue protein, islet amyloid polypeptide (IAPP), as either insoluble or small oligomers, appears to play a direct role in death pancreatic β-islet cells type II diabetes. While IAPP has been known be primary component diabetes amyloid, molecular interactions responsible for this have not identified. To identify aggregation-prone region(s), we constructed library randomly generated point mutants IAPP. This mutant was expressed Escherichia coli genetic fusions...

10.1021/bi100337p article EN Biochemistry 2010-08-10

The aggregation of the amyloidogenic polypeptide IAPP (Islet Amyloid Polypeptide, amylin) is believed to play a direct role in death pancreatic β-islet cells type II diabetes. Preventing initial event one strategy for slowing, and possibly preventing, progression this disease. Here, we investigate myricetin's potential as an inhibitor aggregation. We show that myricetin prevented thioflavin T binding concentration dependent manner. Atomic force microscopy revealed fiber formation under...

10.2174/1874091x01206010066 article EN cc-by The Open Biochemistry Journal 2012-06-27

The misfolding and aggregation of proteins into amyloid has been linked to a variety age-related diseases. Aggregation proteins, such as Aβ in Alzheimer's disease Islet Amyloid Polypeptide (IAPP, amylin) type 2 diabetes, appears lead the formation toxic assemblies. These assemblies range size from small oligomers (2-8 proteins) large fibrils (thousands proteins). It remains unclear how these amyloidogenic misfold form species, but growing evidence suggests that inhibiting could slow, if not...

10.2174/1874070701105010039 article EN The Open Biotechnology Journal 2011-12-23

The polyphenol, 1,2,3,4,6-penta-O-galloyl-β-D-glucose (PGG) has been found to exhibit a host of positive pharmacologic activities, including anti-cancer and anti-diabetic. Little is known about the mode action PGG in yielding these activities. We show here that potent inhibitor IAPP (islet amyloid polypeptide, amylin) aggregation. Preventing initial aggregation event one strategy for slowing, possibly preventing, toxic effects oligomeric intermediates. Equal molar ratios substantially...

10.3109/13506129.2012.762761 article EN Amyloid 2013-01-22

Carbon monoxide binding was studied in a collection of de novo heme proteins derived from combinatorial libraries sequences designed to fold into 4-helix bundles. The design the based on previously reported "binary code" strategy, which patterning polar and nonpolar amino acids is specified explicitly, but exact identities side chains are varied extensively.(1) mixture included histidine methionine, ligate iron natural proteins. However, no attempt made explicitly site. Nonetheless, as...

10.1021/ja0036007 article EN Journal of the American Chemical Society 2001-02-10

Increasing evidence suggests that the aggregation of small peptide Abeta42 plays an important role in development Alzheimer's disease. Inhibiting initial may be effective treatment for preventing, or slowing, onset Using vivo screen based on enzyme EGFP, we have searched through two combinatorially diverse libraries to identify peptides capable inhibiting aggregation. From this screen, three candidate were selected and characterized. ThT studies indicated amyloid Additional showed one was...

10.1002/psc.1150 article EN Journal of Peptide Science 2009-06-26

The aggregation of the 37-amino acid polypeptide human islet amyloid (hIAPP), as either insoluble or small oligomers, appears to play a direct role in death pancreatic β-islet cells type 2 diabetes. hIAPP is considered be one most amyloidogenic proteins known. quick leads formation toxic species, such oligomers and fibers, that damage mammalian (both rat cells). Whether this toxicity necessary for progression diabetes merely side effect disease remains unclear. If into on-path developing...

10.1002/psc.3199 article EN Journal of Peptide Science 2019-06-23

The aggregation of the 37-amino acid polypeptide islet amyloid (IAPP, amylin), as either insoluble or small oligomers, appears to play a direct role in death pancreatic β-islet cells type 2 diabetes. It is believed that inhibiting IAPP may slow down, if not prevent entirely, progression this disease. Extracts 13 different common fruits were analyzed for their ability amyloidogenic IAPP. Thioflavin T binding, immuno-detection and circular dichroism assays performed test vitro inhibitory...

10.1016/j.jff.2014.12.013 article EN cc-by-nc-nd Journal of Functional Foods 2014-12-24

Abstract A seven‐week “gene to protein” laboratory sequence is described for an undergraduate biochemistry course. Student pairs were given the task of introducing a point mutation their choosing into well studied protein, enhanced green fluorescent protein (EGFP). After conducting literature searches, each student group chose they wanted introduce EGFP. Students designed sequence‐specific mutagenic primers and constructed desired mutation. The resulting EGFP mutant proteins expressed in E....

10.1002/bmb.20257 article EN Biochemistry and Molecular Biology Education 2009-03-01

The progression of type 2 diabetes in humans appears to be linked the loss insulin-producing β-cells. One major contributors β-cell is formation toxic human IAPP amyloid (hIAPP, Islet Amyloid Polypeptide, amylin) pancreas. Inhibiting hIAPP could slow, if not prevent altogether, diabetes. Many non-human organisms also express amyloidogenic variants known kill pancreatic cells and give rise diabetes-like symptoms. Surprisingly, some these function as inhibitors aggregation, raising possibility...

10.2174/0109298665340227241115110404 article EN Protein and Peptide Letters 2024-12-10

To identify naturally occurring variants of IAPP capable inhibiting the aggregation human and protecting living cells from toxic effects IAPP.The loss insulin-producing β-cells overall progression type 2 diabetes appears to be linked formation (hIAPP, Islet Amyloid Polypeptide, amylin) amyloid in pancreas. Inhibiting initial hIAPP has potential slow, if not stop entirely, halt disease.To characterize aggregation.Synthetic was incubated with synthetic identified natural sources under...

10.2174/0929866528666210806152706 article EN Protein and Peptide Letters 2021-08-09

Aggregation of the short polypeptide, Islet Amyloid Polypeptide (IAPP, amylin), appears to play a direct role in death pancreatic β‐islet cells type 2 diabetes. Inhibiting aggregation IAPP has potential slow, if not prevent entirely, progression this disease. Extracts thirteen different common fruits were analyzed for their ability amyloidogenic IAPP. Thioflavin T binding, immuno‐detection and circular dichroism assays performed test vitro inhibitory each extract. Atomic force microscopy was...

10.1096/fasebj.29.1_supplement.564.4 article EN The FASEB Journal 2015-04-01

The aggregation of the 37‐amino acid polypeptide human Islet Amyloid Polypeptide (hIAPP, amylin), as either insoluble amyloid or small oligomers, appears to play a direct role in death pancreatic β‐islet cells type 2 diabetes. It is known that several organisms express non‐amyloidogenic variants IAPP (such rat and mouse) are not develop diabetes naturally. Conversely, highly amyloidogenic human, cat primates) Despite significant amount genetic information available, no comprehensive study...

10.1096/fasebj.2018.32.1_supplement.795.6 article EN The FASEB Journal 2018-04-01
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